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User:Johnswift

1,657 bytes added, 25 January
Created page with "Natural endogenous peptides exhibit desirable medicinal properties but are often limited in applications by rapid proteolysis and insufficient membrane permeability. Editing o..."
Natural endogenous peptides exhibit desirable medicinal properties but are often limited in applications by rapid proteolysis and insufficient membrane permeability. Editing of naturally occurring peptide sequences to develop peptidomimetic analogs thus creates a promising class of therapeutic approaches.
Overview of Peptidomimetics
Over the past few decades, a large number of bioactive peptides have been discovered and characterized that influence intercellular communication and control a range of important functions due to their interaction with their membrane-bound receptors. As a result, many bioactive peptides have been prepared on a large scale and tested pharmacologically and clinically, allowing the development of new therapies for various pathologies.

The need for peptidomimetic development stems from the limitations of peptides as potential therapeutics, including:

Limited stability towards proteolysis, resulting in a half time in the order of minutes in the gastrointestinal tract and in serum.
Poor transport properties to the blood and across the blood-brain barrier due to high molecular weight and lack of specific transport systems.
Rapid excretion through the liver and kidneys.
Intrinsic flexibility enables the interaction with multiple proteins besides the target, and thus resulting in undesired side effects.
The structure and function of peptidomimetics have been significantly improved compared with the parent starting peptide, so peptidomimetics have become one of the most potential therapeutic methods.
More details: [https://www.pepdomtech.com/peptidomimetic-development-service.html peptidomimetic development]
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